The intracellular iron repository, ferritin sequesters excess of free iron (II), storing them as iron (III) bio-mineral inside its central nanocavity and thereby acts as antioxidant. The redox reactions involving Fe(II)/Fe(III) ions within the protein shell is expected to be contributing to its electrochemical nature. Iron uptake/release in ferritin can be controlled by describing the mechanism and pathway of electron transfer (ET) which still remains enigmatic. Additionally, the elusive mechanism behind the spontaneous organization of ferritin subunits into hollow, spherical nanocage structure is targeted to be unraveled by tracking the kinetics of ferritin self-assembly using light scattering technique. Moreover, understanding the mechanism of ferritin self-assembly and identification of stable intermediates (ferritin assembly units) will be useful for regulating the process of self-assembly and preparation of hybrid ferritins. Preparation of hybrid ferritin provides a great opportunity to understand the mechanisms of iron loading/unloading, size constrained nanomaterial synthesis and targeted drug delivery. However, the large size (M.W. = 490 kDa) has been limiting the separation of different hybrid ferritin nanocages from each other in their intact assembled form and further characterization. Hence, formation of hybrid ferritin (comprising subunits of wild type (WT) and modified ferritin) nanocages, its integrity and iron loading ability (ferritin activity) were tested and confirmed in native PAGE. Using the current understanding of the structure, self-assembly and electrochemistry of ferritin, the current work aims to engineer ferritin protein nanocages in order to utilize them as potential nanoreactor and nanocarrier.